研究领域
Many of life's most important processes are performed by metalloproteins. Metalloproteins are proteins that contain one or more metal cofactors at their active-sites, and can be thought of as the ultimate transition metal complex. The ligand environment about the metal-center in a metalloprotein is often characterized by low symmetry, an unusual coordination geometry, and unique metal-ligand bonding. Therefore, many of the fine details concerning how interactions between the primary and secondary coordination sphere and the metal ion contribute to the metalloproteins physical properties and function in many metalloproteins remain unclear. To understand these complex and fascinating systems the Shearer group utilizes a multi-tiered approach. We first start by considering the relevant information concerning the metalloprotein in question and design and prepare small transition metal complexes and metallopeptides based on the active-site of the metalloprotein. These metalloprotein synthetic analogues are then subjected to a detailed spectroscopic and computational analysis. Finally the information acquired from these studies are applied back to the metalloprotein. Further studies on the metalloprotein then aid in refining future generations of the synthetic analogues, and the whole process is repeated. Current areas of focus in the Shearer group concern: the biological chemistry of nickel containing metalloproteins, the interaction between copper ions and proteins involved in neurodegenerative disorders, and the biological chemistry of sulfur and selenium containing proteins.
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Fitzpatrick, J.; Kalyvas, H.; Filipovic, M.; Ivanovic-Burmazovic, I.; MacDonald, J.; Shearer, J.; Kim, E. (2014) Transformation of a Mononitrosyl Iron Complex to a [2Fe-2S] Cluster by a Cysteine Analog. Journal of the American Chemical Society. in press
Shearer, J. (2014) Insight Into The Structure and Mechanism of Nickel Containing Superoxide Dismutase Derived From Peptide Based Mimics. Accounts of Chemical Research. in press
Linn, D.; Kieser, J.; Shearer, J. (2014) The Novel Hydrogen-Rich Binuclear Cobalt Complex Anion, [(CoH3)2H3]5-. Dalton Transactions, 43, 3412-3415.
Shearer, J. (2013) Dioxygen and Superoxide Stability of Metallopeptide Based Mimics of Nickel Containing Superoxide Dismutase: The Influence of Amine/Amidate vs. Bis- Amidate Coordination. Journal of Inorganic Biochemistry, 129, 145-149.
Bellow, J.A.; Fang, D.; Kovacevic, N.; Martin, P.D.; Shearer, J.; Cisneros, G.A.; Groysman, S. (2013) Novel Cluster Topologies Featuring Rare Seesaw Geometry at Transition Metal Centers. Chemistry - A European Journal, 19, 12225-12228.
Shearer, J. (2013) Use of Metallopeptide Based Mimics Suggests A Proton Coupled Electron Transfer Mechanism During Superoxide Reduction Facilitated by Nickel Containing Superoxide Dismutase. Angewandte Chemie International Edition, 52, 2569-2572.
Peck, K.L.; Clewett, H.S.; Schmitt, J.C.; Shearer, J. (2013) Influence of the English Amyloid-β Mutation (H6R) on the Binding of Cu(I) to Amyloid-β Oligomers. Chemical Communication, 49, 4749-4799.
Fitzpatrick, J.l Kalyvas, H.; Shearer, J.; Kim, E. (2013) Oxygen Mediated Conversion of {Fe(NO)2}9 Dinitrosyl Iron Complexes to Roussin's Red Esters. Chemical Communications, 49, 5550-5552
Dutta, A; Flores, M.; Roy, S.; Schmitt, J.C.; Hamilton, A.G.; Hartnett, H.E.; Shearer, J.; Jones, A.K. (2013) Sequential Oxidations of Thiolates and the Cobalt Metallocenter in a Synthetic Metallopeptide: Implications for the Biosynthesis of Nitrile Hydratase. Inorganic Chemistry, 52, 5236-5245.
Lim, S.H.; Schmitt, J.C.; Shearer, J.; Jin, J.; Olmstead, M.M.; Fettinger, J.C.; Balch, A.L. (2013) Crystallographic and Computational Studies of Luminescent, Binuclear Gold(I) Complexes, AuI2(Ph2P(CH2)nPPh2)2I2 (n = 3-6). Inorganic Chemistry, 52, 823-831.
Chen, K., Strasser, C. E., Schmitt, J. C., Shearer, J., and Catalano, V. J. (2012) Modulation of Luminescence by Subtle Anion-Cation and Anion-π Interactions in a Trigonal AuI...CuI Complex. Inorganic Chemistry, 51, 1207-1209.
Shearer, J., Callan, P. E. Masitas, C. A. and Grapperhaus, C. (2012) Influence of Sequential Thiolate Oxidation on a Nitrile Hydratase Mimic Probed by Multiedge X-ray Absorption Spectroscopy. Inorganic Chemistry, 51, 6032-6045.
Coggins, M. K., Toledo, S., Shaffer, E., Kaminsky, W., Shearer, J. Kovacs, J. A. (2012) Characterization and Dioxygen Reactivity of a New Series of Coordinatively Unsaturated Thiolate-Ligated Manganese(II) Complexes. Inorganic Chemistry, 51, 6633-6644.
Shakya, R., Allard, M. M., Johann, M., Heeg, M. J., Rentschler, E., Shearer, J. M., McGarvey, B., Verani, C. N. (2011) Modeling the Geometric, Electronic, and Redox Properties of Iron(III)-Containing Amphiphiles with Asymmetric [NN'O] Headgroups. Inorganic Chemistry, 50, 8356-8366.
Tran, N.; Kalyvas, H.; Skodje, K.; Hayashi, T.; Moenne-Loccoz, P.; Callan, P.; Shearer, J.; Kirschenbaum, L.; Kim, E. (2011) Phenol Nitration Induced by a {Fe(NO)2}10 Dinitrosyl Iron Complex. Journal of the American Chemical Society, 133, 1184-1187.
Shearer, J., Rossenkoetter, K. E., Callan, P. E. and Pham, C. (2011) One Octarepeat Expansion to the Human Prion Protein Alters Both the Zn2+ and Cu2+ Coordination Environments Within the Octarepeat Domain. Inorganic Chemistry, 50, 1173-1175.
Shearer, J.; Callan, P. E.; Tran, T.; Szalai, V. S. (2010) Cu K-edge X-ray Absorption Spectroscopy Reveals Differential Copper Coordimation Within Amyloid-β Oligomers Compared to Amyloid-β Monomers. Chemical Communications, 46, 9137-9139.
Shearer, J.; Callan, P. E.; Amie, J. (2010) Metallopeptide Based Mimics Demonstrates That the Metalloprotein Nitrile Hydratase Requires Two Oxidized Cysteinates for Catalytic Activity. Inorganic Chemistry, 49, 9064-9077.
Lesh, F. D.; Shanmugam, R.; Allard, M. M.; Lanznaster, M.; Hegg, M. J.; Rodgers, M. T.; Shearer, J.; Verani, C. N. (2010) A Modular Approach to Redox-active Multimetallic Amphiphiles of Discotic Topology. Inorganic Chemistry, 49, 7226-7228.
Mathrubootham, V., Thomas, J., Staples, R., McCraken, J., Shearer, J., Hegg, E. L. (2010) Bis-amide and Monoamine/amide NiN2S2 Complexes as Models for Nickel Containing Acetyl Coenzyme Synthase and Superoxide Dismutase: An Experimental and Computational Study. Inorganic Chemistry, 49, 5393-5406.
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